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Conserved domains on  [gi|1958784183|ref|XP_038968643|]
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doublecortin domain-containing protein 2C isoform X6 [Rattus norvegicus]

Protein Classification

ubiquitin family protein( domain architecture ID 1000087)

ubiquitin family protein belongs to an diverse class of protein modifier and gene expression regulatory proteins that participate in a number of cellular processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl1_cv_Nsp3_N-like super family cl28922
first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV ...
28-106 3.59e-30

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.


The actual alignment was detected with superfamily member cd17154:

Pssm-ID: 475130  Cd Length: 80  Bit Score: 112.98  E-value: 3.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  28 SRYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKVFP-LGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFKS 106
Cdd:cd17154     1 SRTINVFTNGEVLVPPAKIIIPKFTLRSWENVLAMITEKAFLrTGGVFRLCTLNGHPVSDSTELEDNHYYVAVGSEKFKA 80
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
398-548 1.98e-06

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 50.85  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  398 QTDPSVRQESLEKSSLTQDQRHEQQESfiksslGAPPPEQRPEMKESPRQLFLGPTPPEHQLEQQEIPEQSSFGPPSPEQ 477
Cdd:PRK10263   690 DADAAAEAELARQFAQTQQQRYSGEQP------AGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQ 763
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958784183  478 QLEQQEIPVqlslGPPSPEQQLEQPEIPVQSFLGP-------PSTEQQLEQGSPGQLFLGPSSPKPPEHQFEQQEIPA 548
Cdd:PRK10263   764 QYQQPQQPV----APQPQYQQPQQPVAPQPQYQQPqqpvapqPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 837
 
Name Accession Description Interval E-value
DCX2_DCDC2C cd17154
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
28-106 3.59e-30

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340674  Cd Length: 80  Bit Score: 112.98  E-value: 3.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  28 SRYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKVFP-LGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFKS 106
Cdd:cd17154     1 SRTINVFTNGEVLVPPAKIIIPKFTLRSWENVLAMITEKAFLrTGGVFRLCTLNGHPVSDSTELEDNHYYVAVGSEKFKA 80
DCX pfam03607
Doublecortin;
52-104 8.43e-13

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 63.24  E-value: 8.43e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958784183  52 SLSDWNSVLAMIGEKV--FPLGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESF 104
Cdd:pfam03607   6 RFRSFDALLDELTEKVvkLPFGAVRKLYTLDGKRVTSLDELEDGGVYVAAGREKF 60
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
29-109 1.53e-07

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 49.18  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183   29 RYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKV-FPLG-GVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFKS 106
Cdd:smart00537   6 KRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEVVkLDLPhGVRKLYTLDGKKVTSLDELEDGGSYVASGTEAFKK 85

                   ...
gi 1958784183  107 IPY 109
Cdd:smart00537  86 VDY 88
PRK10263 PRK10263
DNA translocase FtsK; Provisional
398-548 1.98e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 50.85  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  398 QTDPSVRQESLEKSSLTQDQRHEQQESfiksslGAPPPEQRPEMKESPRQLFLGPTPPEHQLEQQEIPEQSSFGPPSPEQ 477
Cdd:PRK10263   690 DADAAAEAELARQFAQTQQQRYSGEQP------AGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQ 763
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958784183  478 QLEQQEIPVqlslGPPSPEQQLEQPEIPVQSFLGP-------PSTEQQLEQGSPGQLFLGPSSPKPPEHQFEQQEIPA 548
Cdd:PRK10263   764 QYQQPQQPV----APQPQYQQPQQPVAPQPQYQQPqqpvapqPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 837
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
386-526 2.73e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 47.34  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 386 LALPETQEKVEVQTDPSVRQESLEKSSLTQDQRHEQQESFIKSSLGAPPPEQRPEMKESPRQlFLGPTPPEHQLE-QQEI 464
Cdd:pfam09770 194 MSLEEVEAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQ-HPGQGHPVTILQrPQSP 272
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958784183 465 PEQSSFGPPSPEQQLEQQEIPVQlslgPPSPEQQLEQPEIPVQSFLGPPSTEQQLEQGSPGQ 526
Cdd:pfam09770 273 QPDPAQPSIQPQAQQFHQQPPPV----PVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAH 330
 
Name Accession Description Interval E-value
DCX2_DCDC2C cd17154
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 ...
28-106 3.59e-30

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2C (DCDC2C); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340674  Cd Length: 80  Bit Score: 112.98  E-value: 3.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  28 SRYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKVFP-LGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFKS 106
Cdd:cd17154     1 SRTINVFTNGEVLVPPAKIIIPKFTLRSWENVLAMITEKAFLrTGGVFRLCTLNGHPVSDSTELEDNHYYVAVGSEKFKA 80
DCX2_DCDC2_like cd16113
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
28-100 1.23e-18

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340530  Cd Length: 74  Bit Score: 80.31  E-value: 1.23e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958784183  28 SRYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKVFP-LGGVRKLFTMDGHLLDDSKNLQDNYFYVAAG 100
Cdd:cd16113     1 PKTIHVFPNGDLLHPPSKVLLTKRRLPNWDTVLEEVTEKVKLqTGAVRKLYTLDGKRISDPDELVNGGQYVAVG 74
DCX pfam03607
Doublecortin;
52-104 8.43e-13

Doublecortin;


Pssm-ID: 460986  Cd Length: 60  Bit Score: 63.24  E-value: 8.43e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958784183  52 SLSDWNSVLAMIGEKV--FPLGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESF 104
Cdd:pfam03607   6 RFRSFDALLDELTEKVvkLPFGAVRKLYTLDGKRVTSLDELEDGGVYVAAGREKF 60
DCX2_DCDC2B cd17153
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 ...
30-105 5.34e-12

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2B (DCDC2B); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of a ubiquitin-like tertiary fold. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340673  Cd Length: 80  Bit Score: 61.69  E-value: 5.34e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958784183  30 YINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKV-FPLGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFK 105
Cdd:cd17153     3 IIHVFRNGDLLSPPFRLLIPKHMLQDWETILSLLTEKAnLRTGAVRKLCTLDGVPLSSGKELVSGQYYVAVGSEKFK 79
DCX cd01617
Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin ...
29-100 5.10e-11

Dublecortin-like domain structurally similar to a beta-grasp ubiquitin-like fold; Dublecortin (DCX) is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. The DCX gene family consists of eleven paralogs in human and mouse, and its DCX protein domains can occur in double tandem or as single DCX repeats. Proteins with DCX tandem domains in general have roles in microtubule (MT) regulation and signal transduction such as X-linked doublecortin (DCX), retinitis pigmentosa-1 (RP1) and doublecortin-like kinase (DCLK). Single DCX repeat proteins are normally localized to actin-rich subcellular structures, or the nucleus such as DCDC2. DCX is not only a unique MAP in terms of structure, it also interacts with multiple additional proteins. Mutations in human DCX genes are associated with abnormal neuronal migration, epilepsy, and mental retardation.


Pssm-ID: 340456  Cd Length: 73  Bit Score: 58.78  E-value: 5.10e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958784183  29 RYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKVFPL-GGVRKLFTMDGHLLDDSKNLQDNYFYVAAG 100
Cdd:cd01617     1 KRITVFRNGDKNFKGVKVLVKPRRFRTFDQLLDELTEKLGLPtGGVRKLYTPSGKLVKSLSDLEDGESYVVCG 73
DCX2_DCDC2 cd17152
Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
53-105 2.69e-10

Doublecortin-like domain 2 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340672  Cd Length: 80  Bit Score: 56.73  E-value: 2.69e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958784183  53 LSDWNSVLAMIGEKV-FPLGGVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFK 105
Cdd:cd17152    26 LNQWEKILEMITEKVtLRTGAVRRLYTLDGKLINDGSELENGQFYVAVGREKFK 79
DCX smart00537
Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the ...
29-109 1.53e-07

Domain in the Doublecortin (DCX) gene product; Tandemly-repeated domain in doublin, the Doublecortin gene product. Proposed to bind tubulin. Doublecortin (DCX) is mutated in human X-linked neuronal migration defects.


Pssm-ID: 214711  Cd Length: 89  Bit Score: 49.18  E-value: 1.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183   29 RYINVFTNGRLFIPPIKIIIPKFSLSDWNSVLAMIGEKV-FPLG-GVRKLFTMDGHLLDDSKNLQDNYFYVAAGLESFKS 106
Cdd:smart00537   6 KRIRFYRNGDRFFKGVRLVVNRKRFKSFEALLQDLTEVVkLDLPhGVRKLYTLDGKKVTSLDELEDGGSYVASGTEAFKK 85

                   ...
gi 1958784183  107 IPY 109
Cdd:smart00537  86 VDY 88
PRK10263 PRK10263
DNA translocase FtsK; Provisional
398-548 1.98e-06

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 50.85  E-value: 1.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  398 QTDPSVRQESLEKSSLTQDQRHEQQESfiksslGAPPPEQRPEMKESPRQLFLGPTPPEHQLEQQEIPEQSSFGPPSPEQ 477
Cdd:PRK10263   690 DADAAAEAELARQFAQTQQQRYSGEQP------AGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQ 763
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958784183  478 QLEQQEIPVqlslGPPSPEQQLEQPEIPVQSFLGP-------PSTEQQLEQGSPGQLFLGPSSPKPPEHQFEQQEIPA 548
Cdd:PRK10263   764 QYQQPQQPV----APQPQYQQPQQPVAPQPQYQQPqqpvapqPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPV 837
DCX1_DCDC2_like cd17071
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and ...
54-105 4.14e-06

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2) and similar proteins; DCDC2 is a member of the doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with stable double tandem DCX repeats of ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340591  Cd Length: 80  Bit Score: 44.90  E-value: 4.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958784183  54 SDWNSVLAMIGEKV-FPLGGVRKLFT-MDGHLLDDSKNLQDNYFYVAAGLESFK 105
Cdd:cd17071    26 RTFDAFLNEVTSGIkAPFGAVRSIYTpTGGHRVKDLDSLQNGGVYVAAGSERFK 79
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
386-526 2.73e-05

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 47.34  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 386 LALPETQEKVEVQTDPSVRQESLEKSSLTQDQRHEQQESFIKSSLGAPPPEQRPEMKESPRQlFLGPTPPEHQLE-QQEI 464
Cdd:pfam09770 194 MSLEEVEAAMRAQAKKPAQQPAPAPAQPPAAPPAQQAQQQQQFPPQIQQQQQPQQQPQQPQQ-HPGQGHPVTILQrPQSP 272
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958784183 465 PEQSSFGPPSPEQQLEQQEIPVQlslgPPSPEQQLEQPEIPVQSFLGPPSTEQQLEQGSPGQ 526
Cdd:pfam09770 273 QPDPAQPSIQPQAQQFHQQPPPV----PVQPTQILQNPNRLSAARVGYPQNPQPGVQPAPAH 330
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
401-581 5.93e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 5.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 401 PSVRQESLEKSSLTQDQRHEQQESFIKSSLGAPPPEQRPEMKE----------SPRQLFLGPTPPEHQLEQQEIPEQSSF 470
Cdd:pfam03154 149 PSPQDNESDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTtqaatagptpSAPSVPPQGSPATSQPPNQTQSTAAPH 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 471 -----GPPSPEQQLEQQEIPVQLSLGPPSPEQQLEQPeIPVQSFLGP-PSTEQQLEQGSPGQLFLGPSSPKPPEHQFEQQ 544
Cdd:pfam03154 229 tliqqTPTLHPQRLPSPHPPLQPMTQPPPPSQVSPQP-LPQPSLHGQmPPMPHSLQTGPSHMQHPVPPQPFPLTPQSSQS 307
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958784183 545 EIPAYSSFGPLSPVQQFEQESSKELSLGlfLEQPPEQ 581
Cdd:pfam03154 308 QVPPGPSPAAPGQSQQRIHTPPSQSQLQ--SQQPPRE 342
PRK10263 PRK10263
DNA translocase FtsK; Provisional
435-548 8.55e-05

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.85  E-value: 8.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  435 PEQRPEMKESPRQLFLGPTPPEHQLEQQEIPEQssfgPPSPEQQLEQQEIPVqlslgppSPEQQLEQPEIPVQsflgPPS 514
Cdd:PRK10263   751 PVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQ----PVAPQPQYQQPQQPV-------APQPQYQQPQQPVA----PQP 815
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958784183  515 TEQQLEQgspgqlflgPSSPKPPEHQFEQQEIPA 548
Cdd:PRK10263   816 QYQQPQQ---------PVAPQPQYQQPQQPVAPQ 840
PRK10263 PRK10263
DNA translocase FtsK; Provisional
463-563 5.05e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 43.15  E-value: 5.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  463 EIPEQSSFGPP-SPEQQLEQQEIP---VQLSLGPPSPEQQLEQPEipvQSFLGPPSTEQQLEQGSPGQLFLGPSSPKPPE 538
Cdd:PRK10263   738 DGPHEPLFTPIvEPVQQPQQPVAPqqqYQQPQQPVAPQPQYQQPQ---QPVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQ 814
                           90       100
                   ....*....|....*....|....*
gi 1958784183  539 HQFEQQEIPAyssfgplSPVQQFEQ 563
Cdd:PRK10263   815 PQYQQPQQPV-------APQPQYQQ 832
PRK10263 PRK10263
DNA translocase FtsK; Provisional
369-545 1.29e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 1.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  369 VPTPEKIRHDILEEKHTLALPETQEKVEVQTDPSVRQESLEKSSLTQDQRHEQQESFIKSSLGAPPPEQRPEMKESPRQL 448
Cdd:PRK10263   346 VASVDVPPAQPTVAWQPVPGPQTGEPVIAPAPEGYPQQSQYAQPAVQYNEPLQQPVQPQQPYYAPAAEQPAQQPYYAPAP 425
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  449 FLGPTPPEHQLEQQEIPEQSSFGPPSPEQQLEQQeiPVQlslgppSPEQQLEQPEIPVQSFLGPPSTEQQ-LEQGSPGQL 527
Cdd:PRK10263   426 EQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQ--STY------QTEQTYQQPAAQEPLYQQPQPVEQQpVVEPEPVVE 497
                          170
                   ....*....|....*...
gi 1958784183  528 FLGPSspKPPEHQFEQQE 545
Cdd:PRK10263   498 ETKPA--RPPLYYFEEVE 513
PHA03378 PHA03378
EBNA-3B; Provisional
432-526 2.49e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 432 APPPEQRPEMKESPrQLFLGPTPPEHQLEQQEIPEQSSFGPPSPEQQLEQQEIPVQLSLGPPSPEQQLEQPEIPVQSFLG 511
Cdd:PHA03378  724 ARPPAAAPGRARPP-AAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQPPPQA 802
                          90
                  ....*....|....*
gi 1958784183 512 PPSTEQQLEQGSPGQ 526
Cdd:PHA03378  803 GPTSMQLMPRAAPGQ 817
PRK10927 PRK10927
cell division protein FtsN;
370-536 2.50e-03

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 40.43  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 370 PTPEKIRHDILEekhtlaLPETQEKVEVQTDPSVRQESLEKSSLTQDQRH--EQQESFIKSS----LGAPPPEQRPEMke 443
Cdd:PRK10927   77 PKPEERWRYIKE------LESRQPGVRAPTEPSAGGEVKTPEQLTPEQRQllEQMQADMRQQptqlVEVPWNEQTPEQ-- 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 444 spRQLFLGPTPPEHQLEQQEIPEQSSFGPPSPEQQLEQ--QEIPVQLSLGPPSPEQQLEqpeiPVQSFLGPP---STEQQ 518
Cdd:PRK10927  149 --RQQTLQRQRQAQQLAEQQRLAQQSRTTEQSWQQQTRtsQAAPVQAQPRQSKPASTQQ----PYQDLLQTPahtTAQSK 222
                         170
                  ....*....|....*...
gi 1958784183 519 LEQGSPgqLFLGPSSPKP 536
Cdd:PRK10927  223 PQQAAP--VTRAADAPKP 238
PRK10263 PRK10263
DNA translocase FtsK; Provisional
401-505 3.30e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 40.45  E-value: 3.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183  401 PSVRQESLEKSSLTQDQRHEQQESfiksSLGAPPPEQRPEMKESPRQLFLGPTPPEHQLEQQEIPEQssfgPPSPEQQLE 480
Cdd:PRK10263   747 PIVEPVQQPQQPVAPQQQYQQPQQ----PVAPQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQ----PVAPQPQYQ 818
                           90       100
                   ....*....|....*....|....*
gi 1958784183  481 QQEIPVqlslGPPSPEQQLEQPEIP 505
Cdd:PRK10263   819 QPQQPV----APQPQYQQPQQPVAP 839
DCX1_DCDC2 cd17149
Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is ...
69-105 4.05e-03

Dublecortin-like domain 1 found in doublecortin domain-containing protein 2 (DCDC2); DCDC2 is a member of doublecortin (DCX) family. It is a microtubule-associated protein (MAP) with a stable ubiquitin-like tertiary fold. Ubiquitin (Ub) is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. Microtubules are key components of the cytoskeleton that are involved in cell movement, shape determination, division and transport. DCDC2 genetic variation in humans is associated with reading disability, attention deficit hyperactivity disorder (ADHD), and difficulties in mathematics. A genetic variant of DCDC2 associates with dyslexia, a common neurobehavioral disorder of reading. DCDC2 protein interacts with many of the same cytoskeleton related proteins that other members of the DCX family interact with.


Pssm-ID: 340669  Cd Length: 80  Bit Score: 36.68  E-value: 4.05e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958784183  69 PLGGVRKLFT-MDGHLLDDSKNLQDNYFYVAAGLESFK 105
Cdd:cd17149    42 PFGAVRNIYTpRGGHRVRSLEQLQSGEQYVAAGRERFK 79
PHA03378 PHA03378
EBNA-3B; Provisional
432-546 6.37e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958784183 432 APPPEQRPEMKESPRQLfLGPTPPEHQLEQQEIPEQSSFGPPSPEQQLEQQEIPVQLSLGP----------PSPEQQLEQ 501
Cdd:PHA03378  704 MRPPAAPPGRAQRPAAA-TGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRarppaaapgaPTPQPPPQA 782
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958784183 502 PEIPVQSFLGPPsTEQQLEQGSPGQLFLGPssPKPPEHQFEQQEI 546
Cdd:PHA03378  783 PPAPQQRPRGAP-TPQPPPQAGPTSMQLMP--RAAPGQQGPTKQI 824
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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